We have designed and synthesized, using the denovo and minimalistic approach, a series of metal-binding proteins with anticipated structural characteristics similar to carbonic anhydrase. Using time-resolved fluorescence lifetime and polarization measurements on these proteins with bound ANS, we have demonstrated a conversion to a more stable, native-like, structural conformational change upon the addition of zinc metal to our buffered solution. The non-metal binding conformer exhibits properties similar to a molten globule intermediate. We continue to change the properties of this metalloprotein in an effort to further optimize the metal-binding characteristics of this system.